Identification |
---|
Name: | Guanylate kinase |
---|
Synonyms: | |
---|
Gene Name: | gmk |
---|
Enzyme Class: | |
---|
Biological Properties |
---|
General Function: | Involved in protein binding |
---|
Specific Function: | Essential for recycling GMP and indirectly, cGMP |
---|
Cellular Location: | Cytoplasm |
---|
SMPDB Pathways: | - purine nucleotides de novo biosynthesis PW000910
- purine nucleotides de novo biosynthesis 1435709748 PW000960
- purine nucleotides de novo biosynthesis 2 PW002033
|
---|
KEGG Pathways: | |
---|
KEGG Reactions: | |
---|
SMPDB Reactions: | |
1.0 | + | 1.0 | → | 1.0Adenosine diphosphate | + | 1.0 | + | 1.0 |
| |
|
---|
EcoCyc Reactions: | |
---|
Complex Reactions: | |
---|
Metabolites: | |
---|
GO Classification: | Function |
---|
catalytic activity | guanylate kinase activity | phosphotransferase activity, phosphate group as acceptor | transferase activity | transferase activity, transferring phosphorus-containing groups | Process |
---|
cellular nitrogen compound metabolic process | metabolic process | nitrogen compound metabolic process | nucleobase, nucleoside and nucleotide metabolic process | nucleobase, nucleoside, nucleotide and nucleic acid metabolic process | nucleoside phosphate metabolic process | nucleotide metabolic process | purine nucleotide metabolic process |
|
---|
Gene Properties |
---|
Blattner: | b3648 |
---|
Gene Orientation | Clockwise |
---|
Centisome Percentage: | 82.32 |
---|
Left Sequence End | 3819451 |
---|
Right Sequence End | 3820074 |
---|
Gene Sequence: | >624 bp
ATGTCAGGTCTGCCACAGGGCAGACCAACGTTTGGCGCTGCGCAAAACGTGAGCGCGGTG
GTGGCGTATGACTTATCTGCCCACATGCTGGATGTCGTGGCACAAGCTGCCGAAGCCCGG
CAACTGAAAAATATCACCACCCGCCAGGGATATGCCGAAAGTCTGCCATTTGCCGATAAC
GCATTTGATATTGTTATCAGCCGTTATTCTGCCCATCACTGGCATGATGTTGGTGCAGCA
CTGCGAGAAGTGAATAGGATATTGAAACCTGGCGGTAGGCTGATTGTGATGGACGTAATG
TCTCCGGGTCACCCAGTGCGCGACATCTGGTTACAGACGGTAGAAGCATTACGCGATACC
TCTCACGTACGAAACTACGCCAGCGGTGAGTGGTTGACGTTAATCAATGAAGCCAATCTG
ATAGTTGATAATTTAATTACAGATAAGTTACCGCTGGAATTTTCTTCATGGGTCGCGAGA
ATGCGTACGCCAGAAGCGTTAGTAGACGCTATTCGCATTTACCAACAGAGCGCATCGACA
GAGGTGAGAACGTATTTTGCCTTGCAGAATGATGGCTTTTTCACCAGTGATATCATCATG
GTAGATGCACATAAAGCGGCATAA |
---|
Protein Properties |
---|
Pfam Domain Function: | |
---|
Protein Residues: | 207 |
---|
Protein Molecular Weight: | 23593 |
---|
Protein Theoretical pI: | 7 |
---|
PDB File: | 1S96 |
Signaling Regions: | |
---|
Transmembrane Regions: | |
---|
Protein Sequence: | >Guanylate kinase
MAQGTLYIVSAPSGAGKSSLIQALLKTQPLYDTQVSVSHTTRQPRPGEVHGEHYFFVNHD
EFKEMISRDAFLEHAEVFGNYYGTSREAIEQVLATGVDVFLDIDWQGAQQIRQKMPHARS
IFILPPSKIELDRRLRGRGQDSEEVIAKRMAQAVAEMSHYAEYDYLIVNDDFDTALTDLK
TIIRAERLRMSRQKQRHDALISKLLAD |
---|
References |
---|
External Links: | |
---|
General Reference: | - Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
- Burland, V., Plunkett, G. 3rd, Daniels, D. L., Blattner, F. R. (1993). "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication." Genomics 16:551-561. Pubmed: 7686882
- Gentry, D., Bengra, C., Ikehara, K., Cashel, M. (1993). "Guanylate kinase of Escherichia coli K-12." J Biol Chem 268:14316-14321. Pubmed: 8390989
- Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
|
---|